Keratins: Difference between revisions
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Section on tertiary structure |
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==Secondary structures of keratins== | ==Secondary structures of keratins== | ||
[[Image:Keratin-secondary-structure-1000px.png | | [[Image:Keratin-secondary-structure-1000px.png|600px|right|thumb| The locations of the α-helical domains (1A, 1B, 2A and 2B) in the central rod of a keratin subunit.]] | ||
The first model of alpha-helix was proposed by Pauling based on the crystallography of wool fibers <ref>PMID:12966187</ref> that were shown to have long helical segments <ref>PMID:6072928</ref>. | The first model of alpha-helix was proposed by Pauling based on the crystallography of wool fibers <ref>PMID:12966187</ref> that were shown to have long helical segments <ref>PMID:6072928</ref>. | ||
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==Tertiary and quaternary structures of keratins== | ==Tertiary and quaternary structures of keratins== | ||
Keratin fibers are difficult to solubilize and so far it has not been possible to crystallize a whole keratin or a combination of keratin polymers. In the face of this difficulty, soluble segments of keratins have been generated both by proteolytic digestion and gene engineering to study the structural properties of keratins <ref name="PMID17521629">PMID:17521629</ref> . | Keratin fibers are difficult to solubilize and so far it has not been possible to crystallize a whole keratin or a combination of keratin polymers. In the face of this difficulty, soluble segments of keratins have been generated both by proteolytic digestion and gene engineering to study the structural properties of keratins <ref name="PMID17521629">PMID:17521629</ref> . | ||
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==References== | ==References== | ||
<references /> | <references /> | ||
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